UniProtKB/Swiss-Prot Q13427: Variant p.Asn699Asp

Peptidyl-prolyl cis-trans isomerase G
Gene: PPIG
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Variant information Variant position:

699 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

LB/B The variants are classified into three categories: LP/P, LB/B and US.

LP/P: likely pathogenic or pathogenic.
LB/B: likely benign or benign.
US: uncertain significance

Residue change:

From Asparagine (N) to Aspartate (D) at position 699 (N699D, p.Asn699Asp). Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.
Physico-chemical properties:

Change from medium size and polar (N) to medium size and acidic (D) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

1 The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:

Lowest score: -4 (low probability of substitution).
Highest score: 11 (high probability of substitution).

More information can be found on the following page
Other resources:

Links to websites of interest for the variant.

Variant rs8207 [ dbSNP | Ensembl ]

Sequence information Variant position:

699 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

754 The length of the canonical sequence.
Location on the sequence:

EKKADRDQSPFSKIKQSSQD N ELKSSMLKNKEDEKIRSSVE The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation:

The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         EKKADRDQSPFSKIKQSSQDNELKSSMLKNKEDEKIRSSVE

Mouse                         EKKADREQSPVSKTKQSSQDNEVKSSTLKNQEDEKTRSPVE

Rat                           EKKADIDQSPVSKTKQSSQDNEVKSSTLKNQEDEKTRSPVE

Xenopus tropicalis            ---------------MMSVDETLMCSFQILKPAEKKKPNAS

Sequence annotation in neighborhood:

The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:

Type: the type of sequence feature.
Positions: endpoints of the sequence feature.
Description: contains additional information about the feature.

Type	Positions	Description
Chain	1 – 754	Peptidyl-prolyl cis-trans isomerase G
Region	182 – 754	Disordered
Modified residue	687 – 687	Phosphoserine
Modified residue	690 – 690	Phosphoserine
Modified residue	696 – 696	Phosphoserine
Cross	693 – 693	Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)
Alternative sequence	358 – 754	Missing. In isoform 2.

Literature citations
RS cyclophilins: identification of an NK-TR1-related cyclophilin.
Nestel F.P.; Colwill K.; Harper S.; Pawson T.; Anderson S.K.;
Gene 180:151-155(1996)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); TISSUE SPECIFICITY; VARIANT ASP-699; A serine/arginine-rich nuclear matrix cyclophilin interacts with the C-terminal domain of RNA polymerase II.
Bourquin J.-P.; Stagljar I.; Meier P.; Moosmann P.; Silke J.; Baechi T.; Georgiev O.; Schaffner W.;
Nucleic Acids Res. 25:2055-2061(1997)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); INTERACTION WITH CLK1 AND RNA POLYMERASE II; DOMAIN; VARIANT ASP-699; ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.
Matsuoka S.; Ballif B.A.; Smogorzewska A.; McDonald E.R. III; Hurov K.E.; Luo J.; Bakalarski C.E.; Zhao Z.; Solimini N.; Lerenthal Y.; Shiloh Y.; Gygi S.P.; Elledge S.J.;
Science 316:1160-1166(2007)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-315 AND SER-696; VARIANT [LARGE SCALE ANALYSIS] ASP-699; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]; Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Olsen J.V.; Vermeulen M.; Santamaria A.; Kumar C.; Miller M.L.; Jensen L.J.; Gnad F.; Cox J.; Jensen T.S.; Nigg E.A.; Brunak S.; Mann M.;
Sci. Signal. 3:RA3-RA3(2010)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-413; SER-415; SER-687; SER-690; SER-696; THR-748 AND SER-753; VARIANT [LARGE SCALE ANALYSIS] ASP-699; IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS];

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.